6ptr

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Current revision (07:35, 11 October 2023) (edit) (undo)
 
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<StructureSection load='6ptr' size='340' side='right'caption='[[6ptr]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='6ptr' size='340' side='right'caption='[[6ptr]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ptr]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PTR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PTR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ptr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bartonella_birtlesii_LL-WM9 Bartonella birtlesii LL-WM9] and [https://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PTR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MLU:N-METHYL-D-LEUCINE'>MLU</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=NZC:N-METHYLIDENE-L-THREONINE'>NZC</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MLU:N-METHYL-D-LEUCINE'>MLU</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=NZC:N-METHYLIDENE-L-THREONINE'>NZC</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6deg|6deg]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ptr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ptr OCA], [https://pdbe.org/6ptr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ptr RCSB], [https://www.ebi.ac.uk/pdbsum/6ptr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ptr ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ptr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ptr OCA], [http://pdbe.org/6ptr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ptr RCSB], [http://www.ebi.ac.uk/pdbsum/6ptr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ptr ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/J1IY24_9RHIZ J1IY24_9RHIZ]] Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.[PIRNR:PIRNR000804]
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[https://www.uniprot.org/uniprot/J1IY24_9HYPH J1IY24_9HYPH] Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.[PIRNR:PIRNR000804]
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==See Also==
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*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bartonella birtlesii LL-WM9]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Streptomyces griseus]]
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[[Category: Antibiotic]]
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[[Category: Broad spectrum]]
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[[Category: Infectious disease]]
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[[Category: Mycobacterium]]
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[[Category: Natural product]]
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[[Category: Niaid]]
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[[Category: Ssgcid]]
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[[Category: Streptomyce]]
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[[Category: Transferase]]
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[[Category: Transferase-antibiotic complex]]
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Current revision

Crystal structure of a DnaN sliding clamp (DNA polymerase III subunit beta) from Bartonella birtlesii bound to griselimycin

PDB ID 6ptr

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